Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen

POKORNÝ, Daniel, Gita JANČAŘÍKOVÁ, Jan KOMÁREK and Michaela WIMMEROVÁ. Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen. In XXV. Biochemický sjezd, 2016. 2016. ISBN 978-80-270-0331-0.

Basic information

• Original name: Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen
• Authors: POKORNÝ, Daniel (203 Czech Republic, belonging to the institution), Gita JANČAŘÍKOVÁ (203 Czech Republic, belonging to the institution), Jan KOMÁREK (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor).
• Edition: XXV. Biochemický sjezd, 2016. 2016.

Other information

• Original language: English
• Type of outcome: Conference abstract
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: Czech Republic
• Confidentiality degree: is not subject to a state or trade secret
• RIV identification code: RIV/00216224:14310/16:00088181
• Organization unit: Faculty of Science
• ISBN: 978-80-270-0331-0
• Keywords (in Czech): lektiny; patogen; photorhabdus; strukturně-funkční charakterizace
• Keywords in English: lectins; pathogen; photorhabdus; structure and function characterization

Abstract

Lectins are ubiquitous carbohydrate-binding proteins found in bacteria, plants, animals, fungi and viruses where they play a key role in various processes. Our research is focused on lectins from Photorhabdus genus - gram-negative bioluminescent bacteria. Photorhabdus genus contains three species all of which are insect pathogens: P. luminescens, P. temperata and P. asymbiotica. Unlike other species in this genus, P. asymbiotica is also able to infect humans. In the P. asymbiotica genome, three genes of putative lectins named PHL, PHL2 and PHL3 were found. Recombinant lectins were studied using broad range of biophysical methods. For affinity measurements we employed isothermal titration calorimetry, micro-scale thermophoresis and surface plasmon resonance. The oligomeric state of the proteins was determined by analytical ultracentrifugation. We have optimized crystallization conditions using high throughput screening, and diffracting-quality crystals were used for structure determination. Structure-supported functional studies help us to understand molecular details of lectin function and their contribution to pathogenesis. Understanding the lectins role in pathogenic processes may be exploited for designing new therapeutic strategies.

Links

• ED1.1.00/02.0068, research and development project: Name: CEITEC - central european institute of technology
• GA13-25401S, research and development project: Name: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu

Investor: Czech Science Foundation